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Product Name: Hsp90alpha (Recombinant, Human, Native sequence)
Catalog #: SPR-101C
Alternative Names: Hsp86, Hsp89A, Hsp90A, Hsp90AA1, HspC1, HspCA, HspCAL3
Type: Recombinant Protein
Accession Number: AJ890083
Gene ID: 3320
SwissProt: P07900
Applications: WB Control
Species: Human
Conjugate/Tag: No tags
Form: Multi-step Chromatographically Purifiied
Storage Buffer: 50mM Tris/HCl pH 7.5, 5mM Bme, 0.3M NaCl, and 10% glycerol
Concentration: 0.75mg/mL
Certificate of Analysis: This product has been certified >90% pure using SDSPAGE analysis.
Background Info: Molecular weight of approximately 90kD
Package Size: 2x 100ug
Storage Temp: -20°C
Shipping Temp: Dry ice, Blue Ice or 4°C
Datasheet: SPR 101 Heat Shock Protein 90Alpha (Hsp90Alpha)
Research Area: Chaperones, Heat Shock, Trafficking
Price: $319.00 USD Add to Cart

SDS PAGE of Hsp90alpha protein.

Research Background: Hsp90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. From a functional perspective, hsp90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (1-4). Despite its label of being a heat-shock protein, hsp90 is one of the most highly expressed proteins in unstressed cells (1–2% of cytosolic protein). It carries out a number of housekeeping functions – including controlling the activity, turnover, and trafficking of a variety of proteins. Most of the hsp90-regulated proteins that have been discovered to date are involved in cell signaling (5-6). The number of proteins now know to interact with Hsp90 is about 100. Target proteins include the kinases v-Src, Wee1, and c-Raf, transcriptional regulators such as p53 and steroid receptors, and the polymerases of the hepatitis B virus and telomerase.5. When bound to ATP, Hsp90 interacts with co-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming a complex that stabilizes and protects target proteins from proteasomal degradation.
In most cases, hsp90-interacting proteins have been shown to co-precipitate with hsp90 when carrying out immunoadsorption studies, and to exist in cytosolic heterocomplexes with it. In a number of cases, variations in hsp90 expression or hsp90 mutation has been shown to degrade signaling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit hsp90 function (7).
References: 1. Arlander SJH, et al. (2003) J Biol Chem 278: 52572-52577.
2. Pearl H, et al. (2001) Adv Protein Chem 59:157-186.
3. Neckers L, et al. (2002) Trends Mol Med 8:S55-S61.
4. Pratt W, Toft D. (2003) Exp Biol Med 228:111-133.
5. Pratt W, Toft D. (1997) Endocr Rev 18: 306–360.
6. Pratt WB. (1998) Proc Soc Exptl Biol Med 217: 420–434.
7. Whitesell L, et al. (1994) Proc Natl Acad Sci USA 91: 8324– 8328.
Cited References: 1. Kathleen M. Gilbert, Benjamin Rowley,Horacio Gomez-Acevedo and Sarah J. Blossom. (2010) Coexposure to Mercury Increases Immunotoxicity of Trichloroethylene. Toxicological Sciences, Volume 119, Issue 2, pp281-292.

2. Mostafa E. Rateb, Wael E. Houssen, Markus Arnold, Mostafa H. Abdelrahman, Hai Deng, William T. A. Harrison, Chinyere K. Okoro, Juan A. Asenjo, Barbara A. Andrews, Gail Ferguson, Alan T. Bull#, Michael Goodfellow, Rainer Ebe, and Marcel Jaspars. Chaxamycins A–D, Bioactive Ansamycins from a Hyper-arid Desert Streptomyces sp. J. Nat. Prod., 2011, 74 (6), pp 1491–1499. DOI: 10.1021/np200320u. Publication Date (Web): May 9, 2011.

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